A DSC study on the effects of various maltodextrins and sucrose on protein changes in frozen-stored minced blue whiting muscle

Herrera, Juan José Rodríguez; Pastoriza, Laura; Sampedro, Gabriel

doi:10.1002/1097-0010(200103)81:4<377::aid-jsfa820>3.0.co;2-0

Cited by 23 publications

(21 citation statements)

References 31 publications

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“…Similar results was reported by Kijowski and Richardson (1996) for washed mechanically deboned poultry meat, this could be explained by concentration of myofibrillar protein by washing and different pH and ionic environment when compared to the raw state of muscle (Wright and Wilding 1984;Xiong et al 1987;Lesiow and Xiong 2001). Analysis of variance of myosin T p showed that myosin's T p varied significantly (P<0.05) as a function of mass fraction of trehalose, but not as of frozen storage time (Sych et al 1990;Herrera et al 2001) (Table 1). These shifts in T p of myosin to the higher values as the mass fraction of trehalose increases can be interpreted as a stabilization of myofibrillar proteins since a higher temperature was required to denature these proteins (Sych et al 1990;Sych et al 1991).…”

Section: Differential Scanning Calorimetrysupporting

confidence: 80%

“…Denaturation enthalpies of myosin and actin for WCM samples with addition of trehalose (w=0-10%), during 360 days of frozen storage, are shown in Table 2. The values of ΔH of myosin and actin showed decrease with the increase of storage time (Sych et al 1990;Herrera et al 2001;Stangierski and Kijowski 2003), highest decreases of ΔH of myosin and actin in all samples were in the first 30 days, especially for sample without additive. Values of ΔH for myosin and actin showed increase with the increase of mass fraction of trehalose, with the exceptions of day 0, which is in agreement with the results reported by Stangierski and Kijowski (2008).…”

Section: Differential Scanning Calorimetrymentioning

confidence: 83%

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Cryoprotective effect of trehalose on washed chicken meat

Kovačević¹,

Mastanjević²

2011

J Food Sci Technol

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The cryoprotective effects of trehalose (w=0-10%) on washed chicken meat (WCM) were investigated. WCM was produced from broiler, frozen and stored for 360 days on −30°C. Myofibrillar protein functional stability was monitored by salt extractable protein (SEP) and differential scanning calorimetry (DSC). Salt extractable protein (SEP) showed that the addition of trehalose caused smaller decrease in protein solubility during frozen storage. Peak thermal transition (T p ) and denaturation enthalpy (ΔH) of myofibrillar proteins were evaluated. Differential scanning calorimetry (DSC) revealed a shift in peak thermal transition temperature (T p ) of myosin and actin to higher temperature as the mass fraction of trehalose increases. The transitions enthalpies of myosin and actin of WCM samples showed higher increase with the increase of mass fraction of trehalose. Since the value of denaturation enthalpy is directly related to amount of native proteins, higher values of ΔH indicates to the higher cryoprotective effects of trehalose.

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Section: Differential Scanning Calorimetrysupporting

confidence: 80%

Section: Differential Scanning Calorimetrymentioning

confidence: 83%

Cryoprotective effect of trehalose on washed chicken meat

Kovačević¹,

Mastanjević²

2011

J Food Sci Technol

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“…As to the samples mixed with maltose, t p of actin transitions vary significantly (P < 0.05) with the increase of the mass fraction (Table 3). t p of myosin shows a greater shift due to the increase of the mass fractions of trehalose and maltose then does t p of actin with all samples and all time intervals (Tables 2 and 3) (Sych et al 1990;Herrera et al 2001). The method of expressing peak enthalpies ΔH was adopted to provide an estimate of the quantity of native proteins.…”

Section: Differential Scanning Calorimetrymentioning

confidence: 87%

“…The analysis of variance of myosin t p showed that myosin t p varied significantly (P < 0.05) as a function of the mass fraction of trehalose, but not as that of frozen storage time (Sych et al 1990) ( Table 2). t p of myosin of WBM samples mixed with maltose varied significantly (P < 0.05) as a function of the mass fraction of trehalose and as a function of time (Table 3) (Herrera et al 2001). These shifts in t p of myosin to higher values as the mass fraction of trehalose and maltose increases can be interpreted as stabilisation of myofibrillar proteins since a higher temperature is required to denature these proteins (Sych et al 1990(Sych et al , 1991.…”

Section: Differential Scanning Calorimetrymentioning

confidence: 96%

Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat

Kovačević¹,

Mastanjević²

2011

Czech J. Food Sci.

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Kovačević D., Mastanjević K. (2011): Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat. Czech J. Food Sci., 29: 15-23.The cryoprotective effects of trehalose and maltose (w = 2-10%) on washed beef meat were investigated. Washed beef meat produced from fresh beef meat was frozen and stored for 360 days at -30°C. Myofibrillar protein functional stability was monitored by salt extractable protein (SEP) and differential scanning calorimetry (DSC). Salt extractable protein (SEP) showed that the addition of trehalose and maltose causeda smaller loss of protein solubility during the frozen storage. Peak thermal transition (t p ) and denaturation enthalpy (ΔH) of myofibrillar proteins were evaluated. Differential scanning calorimetry (DSC) revealed a shift in the peak thermal transition temperature (t p ) of myosin and actin to higher temperature as the mass fractions of trehalose and maltose increased. The transitions enthalpies of myosin and actin of the washed beef meat samples showed a higher increase with the increase of mass fraction of trehalose then of that of maltose. Since the value of denaturation enthalpy is directly related to the amount of native proteins, higher values of ΔH point to higher cryoprotective effects of trehalose.

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“…The denaturation enthalpies of myosin and actin of CMPC samples with addition of barley bran flour, during 180 days of frozen storage, are shown in Figure 1 and 2. The values of ΔH of myosin and actin decreased with increasing of storage time (Herrera et al, 2001;Stangierski and Kijowski, 2008;Kovačević and Mastanjević, 2014). The largest decreases in ΔH of myosin and actin in all samples were in the first 30 Values are means ±SD of triplicate.…”

Section: Thermal Analysismentioning

confidence: 96%

Physico-chemical and thermal properties of chicken myofibrillar protein concentrate (CMPC) mixed with barley bran flour during frozen storage

Mastanjević¹,

Kovačević²

2018

Acta Sci Pol Technol Aliment

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Chicken myofibrillar protein concentrate (CMPC), produced with modified technology used for fish surimi (Dawson et al., 1988;Park et al., 1996), is characterized by very good technological properties, such as a high water retention capacity and a strong ability to form strong gels after being heated. The most frequently used food preservation technique for this kind of product is freezing. Cryoprotectants, such as disaccharides, polysaccharides, polyalcohols, acids and polyphosphates are generally added to surimi to protect myofibrillar proteins from freeze-denaturation during frozen storage and to maintain its high PHYSICO-CHEMICAL AND THERMAL PROPERTIES OF CHICKEN MYOFIBRILLAR PROTEIN CONCENTRATE (CMPC) MIXED WITH BARLEY BRAN FLOUR DURING FROZEN STORAGE ABSTRACTBackground. Possible new additives for surimi-like products made from chicken meat, which could improve its functional properties during frozen storage, are the subject of much research. The use of dietary fibre in surimi-like products made from chicken meat has not been extensively studied. The objective of this study was to determine the effectiveness of barley bran flour in stabilizing chicken myofibrillar proteins during frozen storage and maintaining its functionality. Material and methods. Surimi-like material (chicken myofibrillar protein concentrate -CMPC) from mechanically deboned chicken meat was mixed with barley bran flour (0-6%) and stored in a freezer for 30, 60, 90 and 180 days. Instrumental color measurements (L*, a*, and b* values) were taken using a Hunter-Lab Mini ScanXE. Texture profile analysis (TPA) tests were performed using a TA.XT2i SMS Stable Micro Systems Texture Analyzer) equipped with an aluminium cylindrical probe P/75. Differential scanning calorimetry (DSC) was used for the determination of denaturation temperatures and enthalpies.Results. Denaturation enthalpies of CMPC increased when the mass fraction of barley bran was increased (w = 0-6%). Instrumental color parameters (L*, a* and b*) of CMPC gels were significantly (p < 0.05) affected by the addition of barley bran. Texture profile analysis (TPA) parameters -hardness and chewinessincreased significantly (p < 0.05) with the addition of barley bran (w = 0-6%). Cohesiveness and springiness were also significantly (p < 0.05) affected by the addition of barley bran (w = 0-6%) during frozen storage. Conclusion. The increase in denaturation enthalpies and some instrumental textural and color parameters, indicate possible interactions of chicken myofibrillar proteins with barley bran.

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A DSC study on the effects of various maltodextrins and sucrose on protein changes in frozen-stored minced blue whiting muscle

Cited by 23 publications

References 31 publications

Cryoprotective effect of trehalose on washed chicken meat

Cryoprotective effect of trehalose on washed chicken meat

Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat

Physico-chemical and thermal properties of chicken myofibrillar protein concentrate (CMPC) mixed with barley bran flour during frozen storage

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